References - Homocysteine in Protein Structure/Function and Human Disease - page 147

321. Gerasimova YV, Knorre DD, Shakirov MM, Godovikova TS. Human serum albumin as a
catalyst of RNA cleavage: N-homocysteinylation and N-phosphorylation by oligonucleotide
affinity reagent alter the reactivity of the protein. Bioorg Med Chem Lett. 2008;18
(20):5396-8.
322. Knorre DG, Kudryashova NV, Godovikova TS. Chemical and functional aspects of post-
translational modification of proteins. Acta Naturae. 2009;1(3):29-51.
323. Peters TJ. All about albumin. San Diego, CA: Academic; 1996.
324. Christodoulou J, Sadler PJ, Tucker A. A new structural transition of serum albumin depen-
dent on the state of Cys34. Detection by 1H-NMR spectroscopy. Eur J Biochem. 1994;225
(1):363-8.
325. Gates AT, Lowry M, Fletcher KA, Murugeshu A, Rusin O, Robinson JW, et al. Capillary
electrophoretic screening for the inhibition of homocysteine thiolactone-induced protein
oligomerization. Anal Chem. 2007;79(21):8249-56.
326. Sauls DL, Warren M, Hoffman M. Homocysteinylated fibrinogen forms disulfide-linked
complexes with albumin. Thromb Res. 2011;127(6):576-81.
327. Koopman J, Haverkate F, Grimbergen J, Engesser L, Novakova I, Kerst AF, et al. Abnormal
fibrinogens IJmuiden (B beta Arg14--Cys) and Nijmegen (B beta Arg44--Cys) form
disulfide-linked fibrinogen-albumin complexes. Proc Natl Acad Sci USA. 1992;89
(8):3478-82.
328. Koopman J, Haverkate F, Grimbergen J, Lord ST, Mosesson MW, DiOrio JP, et al. Molecular
basis for fibrinogen Dusart (A alpha 554 Arg- > Cys) and its association with abnormal fibrin
polymerization and thrombophilia. J Clin Invest. 1993;91(4):1637-43.
329. Marchi R, Lundberg U, Grimbergen J, Koopman J, Torres A, de Bosch NB, et al. Fibrinogen
Caracas V, an abnormal fibrinogen with an Aalpha 532 Ser- Cys substitution associated

>

with thrombosis. Thromb Haemost. 2000;84(2):263-70.
330. Hanss M, Biot F. A database for human fibrinogen variants. Ann N Y Acad Sci.
2001;936:89-90.
331. La Corte AL, Ali M, Glowacki R, Jakubowski H, Ridger V, Pease R, et al. In vivo
N-homocysteinylation of fibrinogen and its role in thrombosis. J Thromb Haemost. 2011;9
(SI, Suppl 2):142.
332. Brown MS, Goldstein JL. Lipoprotein metabolism in the macrophage: implications for
cholesterol deposition in atherosclerosis. Annu Rev Biochem. 1983;52:223-61.
333. Steinberg D, Parthasarathy S, Carew TE, Khoo JC, Witztum JL. Beyond cholesterol.
Modifications of low-density lipoprotein that increase its atherogenicity. N Engl J Med.
1989;320(14):915-24.
334. Weisgraber KH, Innerarity TL, Mahley RW. Role of lysine residues of plasma lipoproteins in
high affinity binding to cell surface receptors on human fibroblasts. J Biol Chem. 1978;253
(24):9053-62.
335. Vidal M, Sainte-Marie J, Philippot J, Bienvenue A. Thiolation of low-density lipoproteins
and their interaction with L2C leukemic lymphocytes. Biochimie. 1986;68(5):723-30.
336. Naruszewicz M, Olszewski AJ, Mirkiewicz E, McCully KS. Thiolation of low density
lipoproteins by homocysteine thiolactone causes increased aggregation and altered interac-
tion with cultured macrophages. Nutr Metab Cardiovasc Dis. 1994;4:70-7.
337. Vignini A, Nanetti L, Bacchetti T, Ferretti G, Curatola G, Mazzanti L. Modification induced
by homocysteine and low-density lipoprotein on human aortic endothelial cells: an in vitro
study. J Clin Endocrinol Metab. 2004;89(9):4558-61.
338. Jakubowski H, Boers GH, Strauss KA. Mutations in cystathionine beta-synthase or
methylenetetrahydrofolate reductase gene increase N-homocysteinylated protein levels in
humans. FASEB J. 2008;22(12):4071-6.
339. Strauss KA, Morton DH, Puffenberger EG, Hendrickson C, Robinson DL, Wagner C, et al.
Prevention of brain disease from severe 5,10-methylenetetrahydrofolate reductase deficiency.
Mol Genet Metab. 2007;91(2):165-75.